{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T02:54:03Z","timestamp":1781837643870,"version":"3.54.5"},"reference-count":37,"publisher":"Wiley","issue":"9","license":[{"start":{"date-parts":[[2006,7,17]],"date-time":"2006-07-17T00:00:00Z","timestamp":1153094400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["enviromicro-journals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Environmental Microbiology"],"published-print":{"date-parts":[[2006,9]]},"abstract":"<jats:title>Summary<\/jats:title>\n                  <jats:p>\n                    Besides 19 potential reductive dehalogenase genes, the genome of\n                    <jats:italic>Dehalococcoides ethenogenes<\/jats:italic>\n                    strain 195 contains over 60 genes annotated as encoding oxidoreductases, including five hydrogenase complexes and a formate dehydrogenase (Fdh). Using quantitative reverse transcriptase polymerase chain reaction, we found that genes encoding a periplasmic Hup hydrogenase and the Fdh were the most highly expressed in batch\u2010grown pure cultures, in which the H\n                    <jats:sub>2<\/jats:sub>\n                    partial pressure was &gt;\u200a0.1\u2003atm, and in butyrate\/tetrachloroethene\u2010mixed cultures, in which H\n                    <jats:sub>2<\/jats:sub>\n                    partial pressures were 10\n                    <jats:sup>\u22124<\/jats:sup>\n                    \u221210\n                    <jats:sup>\u22125<\/jats:sup>\n                    \u2003atm. Shotgun electrospray ionization (ESI) and matrix\u2010assisted laser desorption\/ionization (MALDI) tandem mass spectrometry were used to identify multiple peptides in pure culture membrane\u2010enriched fractions matching several highly expressed respiratory enzymes, including three hydrogenases, two reductive dehalogenases, Fdh and DET1407, a 105.5\u2010kDa protein we propose to be part of an S\u2010layer cell wall. Both transcript and mass spectrometric approaches indicated that the putative Fdh was an important oxidoreductase in these cells; nevertheless,\n                    <jats:italic>D.\u2003ethenogenes<\/jats:italic>\n                    cultures could not use formate as an electron donor for reductive dechlorination. Analysis of the gene encoding the large subunit of Fdh indicated that while it was related to other Fdh proteins, its sequence encodes serine rather than cysteine or selenocysteine at a critical position, casting doubt on its function. Overall, genomic and proteomic approaches have provided novel insights into the metabolism of this difficult to culture organism.\n                  <\/jats:p>","DOI":"10.1111\/j.1462-2920.2006.01090.x","type":"journal-article","created":{"date-parts":[[2006,7,17]],"date-time":"2006-07-17T05:48:08Z","timestamp":1153115288000},"page":"1499-1509","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":70,"title":["Transcription and mass\u2010spectroscopic proteomic studies of electron transport oxidoreductases in\n                    <i>Dehalococcoides ethenogenes<\/i>"],"prefix":"10.1111","volume":"8","author":[{"given":"R. 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